ARGL1_HUMAN
ID ARGL1_HUMAN Reviewed; 273 AA.
AC Q9NWB6; B4E0Y3; Q5T257; Q6IQ34;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Arginine and glutamate-rich protein 1;
GN Name=ARGLU1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Embryo, and Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-60 AND SER-77, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP FUNCTION, INTERACTION WITH MED1, AND SUBCELLULAR LOCATION.
RX PubMed=21454576; DOI=10.1074/jbc.m110.206029;
RA Zhang D., Jiang P., Xu Q., Zhang X.;
RT "Arginine and glutamate-rich 1 (ARGLU1) interacts with mediator subunit 1
RT (MED1) and is required for estrogen receptor-mediated gene transcription
RT and breast cancer cell growth.";
RL J. Biol. Chem. 286:17746-17754(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; THR-61 AND SER-77, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76; SER-77 AND SER-266, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Required for the estrogen-dependent expression of ESR1 target
CC genes. Can act in cooperation with MED1. {ECO:0000269|PubMed:21454576}.
CC -!- SUBUNIT: Directly interacts with MED1. {ECO:0000269|PubMed:21454576}.
CC -!- INTERACTION:
CC Q9NWB6; P78362: SRPK2; NbExp=2; IntAct=EBI-2808785, EBI-593303;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21454576}.
CC Note=Recruited, in an estrogen-dependent manner, to ESR1 target gene
CC promoters. Colocalizes with MED1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NWB6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NWB6-2; Sequence=VSP_025674;
CC Name=3;
CC IsoId=Q9NWB6-3; Sequence=VSP_053685, VSP_025674;
CC -!- SIMILARITY: Belongs to the UPF0430 family. {ECO:0000305}.
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DR EMBL; AK001016; BAA91467.1; -; mRNA.
DR EMBL; AK303575; BAG64595.1; -; mRNA.
DR EMBL; AL442127; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050434; AAH50434.1; -; mRNA.
DR EMBL; BC071587; AAH71587.1; -; mRNA.
DR CCDS; CCDS41906.1; -. [Q9NWB6-1]
DR RefSeq; NP_060481.3; NM_018011.3. [Q9NWB6-1]
DR AlphaFoldDB; Q9NWB6; -.
DR SMR; Q9NWB6; -.
DR BioGRID; 120397; 126.
DR IntAct; Q9NWB6; 135.
DR MINT; Q9NWB6; -.
DR STRING; 9606.ENSP00000383059; -.
DR GlyGen; Q9NWB6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NWB6; -.
DR PhosphoSitePlus; Q9NWB6; -.
DR SwissPalm; Q9NWB6; -.
DR BioMuta; ARGLU1; -.
DR DMDM; 74753014; -.
DR EPD; Q9NWB6; -.
DR jPOST; Q9NWB6; -.
DR MassIVE; Q9NWB6; -.
DR MaxQB; Q9NWB6; -.
DR PaxDb; Q9NWB6; -.
DR PeptideAtlas; Q9NWB6; -.
DR PRIDE; Q9NWB6; -.
DR ProteomicsDB; 82923; -. [Q9NWB6-1]
DR ProteomicsDB; 82924; -. [Q9NWB6-2]
DR Antibodypedia; 25410; 86 antibodies from 20 providers.
DR DNASU; 55082; -.
DR Ensembl; ENST00000400198.8; ENSP00000383059.3; ENSG00000134884.15. [Q9NWB6-1]
DR GeneID; 55082; -.
DR KEGG; hsa:55082; -.
DR MANE-Select; ENST00000400198.8; ENSP00000383059.3; NM_018011.4; NP_060481.3.
DR UCSC; uc001vqk.5; human. [Q9NWB6-1]
DR CTD; 55082; -.
DR DisGeNET; 55082; -.
DR GeneCards; ARGLU1; -.
DR HGNC; HGNC:25482; ARGLU1.
DR HPA; ENSG00000134884; Low tissue specificity.
DR MIM; 614046; gene.
DR neXtProt; NX_Q9NWB6; -.
DR OpenTargets; ENSG00000134884; -.
DR PharmGKB; PA162376869; -.
DR VEuPathDB; HostDB:ENSG00000134884; -.
DR eggNOG; ENOG502QPR5; Eukaryota.
DR GeneTree; ENSGT00730000111249; -.
DR HOGENOM; CLU_076749_0_0_1; -.
DR InParanoid; Q9NWB6; -.
DR OMA; YRHSPTI; -.
DR PhylomeDB; Q9NWB6; -.
DR TreeFam; TF324123; -.
DR PathwayCommons; Q9NWB6; -.
DR SignaLink; Q9NWB6; -.
DR BioGRID-ORCS; 55082; 618 hits in 1087 CRISPR screens.
DR ChiTaRS; ARGLU1; human.
DR GeneWiki; ARGLU1; -.
DR GenomeRNAi; 55082; -.
DR Pharos; Q9NWB6; Tdark.
DR PRO; PR:Q9NWB6; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9NWB6; protein.
DR Bgee; ENSG00000134884; Expressed in sural nerve and 201 other tissues.
DR ExpressionAtlas; Q9NWB6; baseline and differential.
DR Genevisible; Q9NWB6; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR InterPro; IPR033371; ARGLU1.
DR PANTHER; PTHR31711; PTHR31711; 1.
DR Pfam; PF15346; ARGLU; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..273
FT /note="Arginine and glutamate-rich protein 1"
FT /id="PRO_0000288438"
FT REGION 1..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..55
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 61
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 16..90
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053685"
FT VAR_SEQ 192..273
FT /note="EEERAKREELERILEENNRKIAEAQAKLAEEQLRIVEEQRKIHEERMKLEQE
FT RQRQQKEEQKIILGKGKSRPKLSFSLKTQD -> VTLGRLESRDSPWQNFQCWVLPPAQ
FT FRKRWNTDYLIPFSSKLNIAAKVNFLAYSEVLTDNLKVGSFYKTYSRILFDLMELAI
FT (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_025674"
SQ SEQUENCE 273 AA; 33216 MW; 70B88496BF18AAE0 CRC64;
MGRSRSRSSS RSKHTKSSKH NKKRSRSRSR SRDKERVRKR SKSRESKRNR RRESRSRSRS
TNTAVSRRER DRERASSPPD RIDIFGRTVS KRSSLDEKQK REEEEKKAEF ERQRKIRQQE
IEEKLIEEET ARRVEELVAK RVEEELEKRK DEIEREVLRR VEEAKRIMEK QLLEELERQR
QAELAAQKAR EEEERAKREE LERILEENNR KIAEAQAKLA EEQLRIVEEQ RKIHEERMKL
EQERQRQQKE EQKIILGKGK SRPKLSFSLK TQD
